カツオ肝臓のNAD(P)加水分解酵素-4-alkaline phosphataseの単離精製とその諸性質〔英文〕

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Two alkaline phosphatase components were isolated from skipjack liver and purified about 12, 000-fold. Their molecular weights were estimated to be 90, 000. They were demonstrated to be composed of a single polypeptide chain.Both components gave optimum pH values at around 8.8. They were activated by divalent metal ions such as Mg2+, Mn2+, and Ca2+, but inhibited by Zn2+, Cu2+, and NH4+. Several chelating agents which were tested exhibited a strong inhibition which was partially recovered by addition of Mg2+. They were also inhibited by arsenate and inorganic orthophosphate, but not by L-tryptophan or L-phenylalanine. The inhibitions caused by nicotinamide, NAD, and NADH2 were all found to be of the mixed type. Both components showed a remarkably low substrate specificity: they acted upon nicotinamide mononucleotide, ATP, ADP, and inorganic pyrophosphate. Both components widely differed from each other only in the Km and Vmax values for each substrate. They showed a weak transphosphorylase activity.
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